کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1964989 1058644 2006 12 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Oncostatin M-induced activation of stress-activated MAP kinases depends on tyrosine 861 in the OSM receptor and requires Jak1 but not Src kinases
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Oncostatin M-induced activation of stress-activated MAP kinases depends on tyrosine 861 in the OSM receptor and requires Jak1 but not Src kinases
چکیده انگلیسی

We have investigated the molecular mechanisms involved in the activation process of the stress-activated protein kinases (SAPK) p38 and JNK in response to the interleukin-6-type cytokine oncostatin M (OSM). Interestingly, activation of p38 and JNK originates from tyrosine residue 861 in the OSMR; the same tyrosine residue which we identified before to be involved in the activation of the mitogen-activated kinases Erk1/2 [Hermanns, H. M., Radtke, S., Schaper, F., Heinrich, P. C., and Behrmann, I. (2000) J. Biol. Chem. 275, 40742–40748]. Therefore, activation of members belonging to all three MAPK families is mediated by one tyrosine motif in the cytoplasmic region of the human OSMR. Concomitantly, point mutation of this residue abrogates the phosphorylation of these kinases. The Janus kinase Jak1 is absolutely essential for the activation of p38 in response to OSM, while Src kinase family members appear to be generally dispensable. Finally, we demonstrate that mutation of tyrosine 861 abrogates OSMR-mediated cell proliferation and identify Erk1/2 as mainly responsible for the proliferative effect. Erk1/2 activation is negatively influenced by p38 activation and inhibition of p38 significantly prolongs the half-life of OSM-induced Egr-1.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Cellular Signalling - Volume 18, Issue 1, January 2006, Pages 50–61
نویسندگان
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